IE65588B1 - Polypeptide inhibitor of viral replication - Google Patents

Polypeptide inhibitor of viral replication

Info

Publication number: IE65588B1
Authority: IE; Ireland
Prior art keywords: vmw; polypeptide; sequence; amino acids; terminal
Prior art date: 1989-07-25

Application number

IE268590A

Other languages

English (en)

Other versions

IE902685A1 (en

Inventor

Richard Francis Greaves

Peter Francis Joseph O'hara

Original Assignee

British Tech Group

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

1989-07-25

Filing date

1990-07-24

Publication date

1995-11-01

1990-07-24 Application filed by British Tech Group filed Critical British Tech Group

1991-02-27 Publication of IE902685A1 publication Critical patent/IE902685A1/en

1995-11-01 Publication of IE65588B1 publication Critical patent/IE65588B1/en

Links

108090000765 processed proteins & peptides Proteins 0.000 title claims abstract description 33
229920001184 polypeptide Polymers 0.000 title claims abstract description 31
102000004196 processed proteins & peptides Human genes 0.000 title claims abstract description 31
239000003112 inhibitor Substances 0.000 title claims description 9
230000029812 viral genome replication Effects 0.000 title description 3
108090000623 proteins and genes Proteins 0.000 claims abstract description 29
150000001413 amino acids Chemical group 0.000 claims abstract description 23
102000004169 proteins and genes Human genes 0.000 claims abstract description 13
241000700605 Viruses Species 0.000 claims abstract description 8
ABHIXYDMILIUKV-CIUDSAMLSA-N Lys-Asn-Asn Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O ABHIXYDMILIUKV-CIUDSAMLSA-N 0.000 claims abstract description 7
241000700584 Simplexvirus Species 0.000 claims abstract description 7
230000010076 replication Effects 0.000 claims abstract description 4
JAMAWBXXKFGFGX-KZVJFYERSA-N Ala-Arg-Thr Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H]([C@@H](C)O)C(O)=O JAMAWBXXKFGFGX-KZVJFYERSA-N 0.000 claims abstract 4
230000006698 induction Effects 0.000 claims description 12
210000004899 c-terminal region Anatomy 0.000 claims description 7
238000013518 transcription Methods 0.000 claims description 7
230000035897 transcription Effects 0.000 claims description 7
230000002401 inhibitory effect Effects 0.000 claims description 6
238000000034 method Methods 0.000 claims description 6
241000700588 Human alphaherpesvirus 1 Species 0.000 claims description 5
230000001413 cellular effect Effects 0.000 claims description 5
FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims description 4
108010068250 Herpes Simplex Virus Protein Vmw65 Proteins 0.000 claims description 4
QRIYOHQJRDHFKF-UWJYBYFXSA-N Ala-Tyr-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)C)CC1=CC=C(O)C=C1 QRIYOHQJRDHFKF-UWJYBYFXSA-N 0.000 claims description 3
SGYSTDWPNPKJPP-GUBZILKMSA-N Arg-Ala-Arg Chemical compound NC(=N)NCCC[C@H](N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(O)=O SGYSTDWPNPKJPP-GUBZILKMSA-N 0.000 claims description 3
QAXCZGMLVICQKS-SRVKXCTJSA-N Arg-Glu-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCN=C(N)N)N QAXCZGMLVICQKS-SRVKXCTJSA-N 0.000 claims description 3
NAPNAGZWHQHZLG-ZLUOBGJFSA-N Asp-Asp-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)N NAPNAGZWHQHZLG-ZLUOBGJFSA-N 0.000 claims description 3
PDQDCFBVYXEFSD-SRVKXCTJSA-N Leu-Leu-Asp Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O PDQDCFBVYXEFSD-SRVKXCTJSA-N 0.000 claims description 3
BMVFXOQHDQZAQU-DCAQKATOSA-N Leu-Pro-Asp Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(=O)O)C(=O)O)N BMVFXOQHDQZAQU-DCAQKATOSA-N 0.000 claims description 3
AZGZDDNKFFUDEH-QWRGUYRKSA-N Tyr-Gly-Ser Chemical compound OC[C@@H](C(O)=O)NC(=O)CNC(=O)[C@@H](N)CC1=CC=C(O)C=C1 AZGZDDNKFFUDEH-QWRGUYRKSA-N 0.000 claims description 3
108010087924 alanylproline Proteins 0.000 claims description 3
108010040443 aspartyl-aspartic acid Proteins 0.000 claims description 3
108010040030 histidinoalanine Proteins 0.000 claims description 3
239000000203 mixture Substances 0.000 claims description 3
LSPKYLAFTPBWIL-BYPYZUCNSA-N Glu-Gly Chemical compound OC(=O)CC[C@H](N)C(=O)NCC(O)=O LSPKYLAFTPBWIL-BYPYZUCNSA-N 0.000 claims description 2
239000003701 inert diluent Substances 0.000 claims description 2
238000011200 topical administration Methods 0.000 claims description 2
XTCNBOBTROGWMW-RWRJDSDZSA-N Thr-Ile-Glu Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)[C@H]([C@@H](C)O)N XTCNBOBTROGWMW-RWRJDSDZSA-N 0.000 claims 1
238000009472 formulation Methods 0.000 claims 1
238000007911 parenteral administration Methods 0.000 claims 1
230000001225 therapeutic effect Effects 0.000 abstract description 2
235000001014 amino acid Nutrition 0.000 description 16
235000018102 proteins Nutrition 0.000 description 9
210000004027 cell Anatomy 0.000 description 7
238000003556 assay Methods 0.000 description 6
101150102264 IE gene Proteins 0.000 description 5
230000015572 biosynthetic process Effects 0.000 description 5
239000000284 extract Substances 0.000 description 5
230000006870 function Effects 0.000 description 5
230000009918 complex formation Effects 0.000 description 4
230000014509 gene expression Effects 0.000 description 4
108020004414 DNA Proteins 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
230000002860 competitive effect Effects 0.000 description 3
238000012217 deletion Methods 0.000 description 3
230000037430 deletion Effects 0.000 description 3
238000011534 incubation Methods 0.000 description 3
230000005764 inhibitory process Effects 0.000 description 3
230000003993 interaction Effects 0.000 description 3
230000002103 transcriptional effect Effects 0.000 description 3
238000011144 upstream manufacturing Methods 0.000 description 3
108020005202 Viral DNA Proteins 0.000 description 2
230000000694 effects Effects 0.000 description 2
238000002474 experimental method Methods 0.000 description 2
239000000499 gel Substances 0.000 description 2
230000000977 initiatory effect Effects 0.000 description 2
238000003780 insertion Methods 0.000 description 2
230000037431 insertion Effects 0.000 description 2
108020004999 messenger RNA Proteins 0.000 description 2
239000002773 nucleotide Substances 0.000 description 2
125000003729 nucleotide group Chemical group 0.000 description 2
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 2
239000000047 product Substances 0.000 description 2
239000000523 sample Substances 0.000 description 2
JKMHFZQWWAIEOD-UHFFFAOYSA-N 2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid Chemical compound OCC[NH+]1CCN(CCS([O-])(=O)=O)CC1 JKMHFZQWWAIEOD-UHFFFAOYSA-N 0.000 description 1
101150021183 65 gene Proteins 0.000 description 1
241000972773 Aulopiformes Species 0.000 description 1
241000701844 Bacillus virus phi29 Species 0.000 description 1
108091003079 Bovine Serum Albumin Proteins 0.000 description 1
102000014914 Carrier Proteins Human genes 0.000 description 1
108091026890 Coding region Proteins 0.000 description 1
108020004705 Codon Proteins 0.000 description 1
238000012287 DNA Binding Assay Methods 0.000 description 1
230000004543 DNA replication Effects 0.000 description 1
102000052510 DNA-Binding Proteins Human genes 0.000 description 1
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 1
108700039691 Genetic Promoter Regions Proteins 0.000 description 1
239000007995 HEPES buffer Substances 0.000 description 1
208000004898 Herpes Labialis Diseases 0.000 description 1
208000029433 Herpesviridae infectious disease Diseases 0.000 description 1
101710192606 Latent membrane protein 2 Proteins 0.000 description 1
108091028043 Nucleic acid sequence Proteins 0.000 description 1
206010067152 Oral herpes Diseases 0.000 description 1
101710186352 Probable membrane antigen 3 Proteins 0.000 description 1
101710181078 Probable membrane antigen 75 Proteins 0.000 description 1
KDCGOANMDULRCW-UHFFFAOYSA-N Purine Natural products N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 1
108091081024 Start codon Proteins 0.000 description 1
101710178472 Tegument protein Proteins 0.000 description 1
101710109576 Terminal protein Proteins 0.000 description 1
239000002253 acid Substances 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
238000000376 autoradiography Methods 0.000 description 1
230000027455 binding Effects 0.000 description 1
108091008324 binding proteins Proteins 0.000 description 1
229940098773 bovine serum albumin Drugs 0.000 description 1
239000000872 buffer Substances 0.000 description 1
210000000234 capsid Anatomy 0.000 description 1
101150055766 cat gene Proteins 0.000 description 1
210000003855 cell nucleus Anatomy 0.000 description 1
108091092356 cellular DNA Proteins 0.000 description 1
239000007795 chemical reaction product Substances 0.000 description 1
230000001055 chewing effect Effects 0.000 description 1
230000006957 competitive inhibition Effects 0.000 description 1
239000006071 cream Substances 0.000 description 1
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 1
238000001514 detection method Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
238000003745 diagnosis Methods 0.000 description 1
LOKCTEFSRHRXRJ-UHFFFAOYSA-I dipotassium trisodium dihydrogen phosphate hydrogen phosphate dichloride Chemical compound P(=O)(O)(O)[O-].[K+].P(=O)(O)([O-])[O-].[Na+].[Na+].[Cl-].[K+].[Cl-].[Na+] LOKCTEFSRHRXRJ-UHFFFAOYSA-I 0.000 description 1
238000001727 in vivo Methods 0.000 description 1
208000015181 infectious disease Diseases 0.000 description 1
238000005259 measurement Methods 0.000 description 1
239000012528 membrane Substances 0.000 description 1
210000004940 nucleus Anatomy 0.000 description 1
239000002674 ointment Substances 0.000 description 1
239000002953 phosphate buffered saline Substances 0.000 description 1
229920002401 polyacrylamide Polymers 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
125000000561 purinyl group Chemical group N1=C(N=C2N=CNC2=C1)* 0.000 description 1
238000011160 research Methods 0.000 description 1
235000019515 salmon Nutrition 0.000 description 1
238000009738 saturating Methods 0.000 description 1
238000003786 synthesis reaction Methods 0.000 description 1
238000012360 testing method Methods 0.000 description 1
241001529453 unidentified herpesvirus Species 0.000 description 1
210000002845 virion Anatomy 0.000 description 1
230000003612 virological effect Effects 0.000 description 1
238000001262 western blot Methods 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
- A61P31/12—Antivirals
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N2710/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA dsDNA viruses
- C12N2710/00011—Details
- C12N2710/16011—Herpesviridae
- C12N2710/16611—Simplexvirus, e.g. human herpesvirus 1, 2
- C12N2710/16622—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/82—Proteins from microorganisms
- Y10S530/826—Viruses
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/22—Viral peptide or viral protein
- Y10S930/224—Herpes related

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Virology (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Molecular Biology (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Biochemistry (AREA)
Gastroenterology & Hepatology (AREA)
General Chemical & Material Sciences (AREA)
Oncology (AREA)
Veterinary Medicine (AREA)
Animal Behavior & Ethology (AREA)
Pharmacology & Pharmacy (AREA)
Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
Chemical Kinetics & Catalysis (AREA)
Public Health (AREA)
Communicable Diseases (AREA)
Peptides Or Proteins (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Medicines Containing Antibodies Or Antigens For Use As Internal Diagnostic Agents (AREA)

IE268590A 1989-07-25 1990-07-24 Polypeptide inhibitor of viral replication IE65588B1 (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
GB898917029A GB8917029D0 (en)	1989-07-25	1989-07-25	Polypeptide inhibitor of viral replication

Publications (2)

Publication Number	Publication Date
IE902685A1 IE902685A1 (en)	1991-02-27
IE65588B1 true IE65588B1 (en)	1995-11-01

Family

ID=10660615

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IE268590A IE65588B1 (en)	1989-07-25	1990-07-24	Polypeptide inhibitor of viral replication

Country Status (11)

Country	Link
US (1)	US5245010A (de)
EP (2)	EP0410713A1 (de)
JP (1)	JPH05505387A (de)
AT (1)	ATE108802T1 (de)
AU (1)	AU637389B2 (de)
CA (1)	CA2063801A1 (de)
DE (1)	DE69010910T2 (de)
GB (2)	GB8917029D0 (de)
IE (1)	IE65588B1 (de)
WO (1)	WO1991001329A1 (de)
ZA (1)	ZA905809B (de)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5633152A (en) *	1988-06-24	1997-05-27	Carnegie Institution Of Washington	Method of controlling viral growth
CA2088600C (en) *	1990-08-02	1999-11-16	Rae L. Burke	Herpes simplex virus vp16 vaccines
GB9119940D0 (en) *	1991-09-18	1991-10-30	Hare Peter F J O	Polypeptide inhibitor of viral replication
AU699168B2 (en) *	1993-07-09	1998-11-26	University Of Pittsburgh	Selection and use of antiviral peptides
AU2587795A (en) *	1994-05-20	1995-12-18	Tularik Inc.	Epstein-barr virus transcription factor binding assay
US8541002B2 (en)	2003-09-12	2013-09-24	Agenus Inc.	Vaccine for treatment and prevention of herpes simplex virus infection

1989
- 1989-07-25 GB GB898917029A patent/GB8917029D0/en active Pending
1990
- 1990-07-24 ZA ZA905809A patent/ZA905809B/xx unknown
- 1990-07-24 IE IE268590A patent/IE65588B1/en not_active IP Right Cessation
- 1990-07-25 US US07/820,658 patent/US5245010A/en not_active Expired - Fee Related
- 1990-07-25 AU AU60710/90A patent/AU637389B2/en not_active Ceased
- 1990-07-25 CA CA002063801A patent/CA2063801A1/en not_active Abandoned
- 1990-07-25 AT AT90911594T patent/ATE108802T1/de not_active IP Right Cessation
- 1990-07-25 WO PCT/GB1990/001143 patent/WO1991001329A1/en not_active Ceased
- 1990-07-25 JP JP90510899A patent/JPH05505387A/ja active Pending
- 1990-07-25 EP EP90308135A patent/EP0410713A1/de active Pending
- 1990-07-25 EP EP90911594A patent/EP0484406B1/de not_active Expired - Lifetime
- 1990-07-25 GB GB9016377A patent/GB2234246B/en not_active Expired - Lifetime
- 1990-07-25 DE DE69010910T patent/DE69010910T2/de not_active Expired - Fee Related

Also Published As

Publication number	Publication date
WO1991001329A1 (en)	1991-02-07
GB2234246A (en)	1991-01-30
GB2234246B (en)	1993-03-17
GB9016377D0 (en)	1990-09-12
IE902685A1 (en)	1991-02-27
DE69010910D1 (de)	1994-08-25
ZA905809B (en)	1992-03-25
DE69010910T2 (de)	1994-12-01
EP0484406A1 (de)	1992-05-13
AU6071090A (en)	1991-02-22
ATE108802T1 (de)	1994-08-15
EP0484406B1 (de)	1994-07-20
US5245010A (en)	1993-09-14
JPH05505387A (ja)	1993-08-12
EP0410713A1 (de)	1991-01-30
AU637389B2 (en)	1993-05-27
CA2063801A1 (en)	1991-01-26
GB8917029D0 (en)	1989-09-13

Legal Events

Date	Code	Title	Description
1999-03-10	MM4A	Patent lapsed

Publication	Publication Date	Title
US5650488A (en)	1997-07-22	Polypeptide inhibitor of the replication of HSV
Smibert et al.	1994	Herpes simplex virus VP16 forms a complex with the virion host shutoff protein vhs
Ikeda et al.	1993	Identification of distinct roles for separate Ela domains in disruption of E2F complexes
De Togni et al.	1988	Detection of fos protein during osteogenesis by monoclonal antibodies
Rice et al.	1995	Herpes simplex virus immediate-early protein ICP22 is required for viral modification of host RNA polymerase II and establishment of the normal viral transcription program
AU669843B2 (en)	1996-06-27	Repressors of the trans-activating function of papillomavirus E2 proteins
Fraefel et al.	1994	Identification and zinc dependence of the bovine herpesvirus 1 transactivator protein BICP0
EP0784686B1 (de)	2006-04-26	Variante von herpesvirus-glycoprotein d
EP0917576A1 (de)	1999-05-26	Wirkstoffe gegen herpesvirus und verfahren zu ihrer identifikation.
Gibson et al.	1990	Identification of precursor to cytomegalovirus capsid assembly protein and evidence that processing results in loss of its carboxy-terminal end
JP2008188017A (ja)	2008-08-21	エプスタイン−バールウイルスペプチド及び該ペプチドに対する抗体
US6337074B1 (en)	2002-01-08	Anti-herpesviral agent
US5821339A (en)	1998-10-13	Compositions and methods for treatment of herpesvirus infections
JPH11308998A (ja)	1999-11-09	単純ヘルペスウイルスのｖｐ１６のワクチン
US4952674A (en)	1990-08-28	Vaccine against varicella-zoster virus
AU637389B2 (en)	1993-05-27	Polypeptide inhibitor of viral replication
Derbigny et al.	2000	The EICP22 protein of equine herpesvirus 1 physically interacts with the immediate-early protein and with itself to form dimers and higher-order complexes
Peden et al.	1998	Effects of mutations within the SV40 large T antigen ATPase/p53 binding domain on viral replication and transformation
Conner et al.	1995	Intracellular localisation of herpes simplex virus type 1 ribonucleotide reductase subunits during infection of cultured cells
Montano et al.	1989	Monoclonal antibody analysis of simian virus 40 small t-antigen expression in infected and transformed cells
HK1001164B (en)	2002-06-14	Epstein-barr virus peptides and antibodies against these peptides